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Directing Proteins to the Rough Endoplasmic Reticulum

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The organelle-specific signaling sequences direct proteins synthesized in the cytosol to their final destination like ER, mitochondria, peroxisomes, etc. Some of the proteins directed to ER are then trafficked via vesicles to other organelles within the cell or the extracellular environment through the Golgi complex. For example, the rough ER synthesizes soluble proteins for transportation to the lysosomes or secretion out of the cell. It can also synthesize transmembrane proteins that can...

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Targeting proteins to the ER
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Updated: May 10, 2026

Using SecM Arrest Sequence as a Tool to Isolate Ribosome Bound Polypeptides

Using SecM Arrest Sequence as a Tool to Isolate Ribosome Bound Polypeptides

Published on: June 19, 2012

Dynamic enzyme docking to the ribosome coordinates N-terminal processing with polypeptide folding.

Arzu Sandikci¹, Felix Gloge, Michael Martinez

¹Zentrum für Molekulare Biologie der Universität Heidelberg, Germany.

Nature Structural & Molecular Biology

|June 18, 2013

Summary

Newly synthesized proteins are processed by enzymes like methionine aminopeptidase (MAP) and peptide deformylase (PDF) at the ribosome. Their rapid binding ensures correct N-terminal processing before folding occurs.

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Single Molecule Fluorescence Energy Transfer Study of Ribosome Protein Synthesis

Single Molecule Fluorescence Energy Transfer Study of Ribosome Protein Synthesis

Published on: July 6, 2021

Area of Science:

Molecular Biology
Biochemistry
Cell Biology

Background:

Newly synthesized polypeptides undergo cotranslational modifications essential for function.
The precise timing and coordination of these early maturation steps remain poorly understood.

Purpose of the Study:

To investigate the spatial and temporal coordination of N-terminal enzymatic processing of nascent polypeptides.
To elucidate the role of Escherichia coli methionine aminopeptidase (MAP) and peptide deformylase (PDF) in ribosome association and nascent-chain processing.

Main Methods:

Investigated the interaction of MAP with ribosomes using biochemical assays.
Analyzed the kinetics of PDF and MAP association/dissociation with ribosomes.
Assessed the impact of chaperone (trigger factor) binding and polypeptide folding on processing efficiency.

Main Results:

Escherichia coli methionine aminopeptidase (MAP) binds to ribosomes via a charged loop critical for processing and cell viability.
MAP competes with peptide deformylase (PDF) for binding sites at the ribosomal tunnel exit.
PDF exhibits rapid association and dissociation kinetics, ensuring timely processing of emerging nascent chains.
Early chaperone recruitment or polypeptide folding hinders N-terminal processing efficiency.

Conclusions:

The rapid ribosome association kinetics of PDF and MAP are vital for temporally separating N-terminal processing from later events like chaperone binding and folding.
This temporal separation ensures the correct maturation pathway for newly synthesized polypeptides.